ID   CDK1_ORYCU              Reviewed;         303 AA.
AC   Q9DGA5;
DT   27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   27-MAR-2024, entry version 104.
DE   RecName: Full=Cyclin-dependent kinase 1;
DE            Short=CDK1;
DE            EC=2.7.11.22 {ECO:0000250|UniProtKB:P06493};
DE            EC=2.7.11.23 {ECO:0000250|UniProtKB:P11440};
DE   AltName: Full=Cell division control protein 2 homolog;
DE   AltName: Full=Cell division protein kinase 1;
DE   AltName: Full=p34 protein kinase;
GN   Name=cdk1; Synonyms=cdc2;
OS   Oryzias curvinotus (Hynann ricefish) (Aplocheilus curvinotus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC   Oryzias.
OX   NCBI_TaxID=104658;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Ovary;
RA   Yamashita M., Mita K.;
RT   "cDNA cloning of Cdc2 and cyclin B in medaka species.";
RL   Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Plays a key role in the control of the eukaryotic cell cycle
CC       by modulating the centrosome cycle as well as mitotic onset; promotes
CC       G2-M transition via association with multiple interphase cyclins (By
CC       similarity). During G2 and early mitosis, CDC25A/B/C-mediated
CC       dephosphorylation activates CDK1/cyclin complexes which phosphorylate
CC       several substrates that trigger at least centrosome separation, Golgi
CC       dynamics, nuclear envelope breakdown and chromosome condensation. Once
CC       chromosomes are condensed and aligned at the metaphase plate, CDK1
CC       activity is switched off by WEE1- and PKMYT1-mediated phosphorylation
CC       to allow sister chromatid separation, chromosome decondensation,
CC       reformation of the nuclear envelope and cytokinesis (By similarity).
CC       Catalyzes lamin (LMNA, LMNB1 and LMNB2) phosphorylation at the onset of
CC       mitosis, promoting nuclear envelope breakdown (By similarity).
CC       {ECO:0000250|UniProtKB:P06493, ECO:0000250|UniProtKB:P13863}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.22;
CC         Evidence={ECO:0000250|UniProtKB:P06493};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.22; Evidence={ECO:0000250|UniProtKB:P06493};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[DNA-directed RNA polymerase] + ATP = ADP + H(+) + phospho-
CC         [DNA-directed RNA polymerase]; Xref=Rhea:RHEA:10216, Rhea:RHEA-
CC         COMP:11321, Rhea:RHEA-COMP:11322, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43176, ChEBI:CHEBI:68546,
CC         ChEBI:CHEBI:456216; EC=2.7.11.23;
CC         Evidence={ECO:0000250|UniProtKB:P11440};
CC   -!- ACTIVITY REGULATION: Phosphorylation at Thr-14 or Tyr-15 inactivates
CC       the enzyme, while phosphorylation at Thr-161 activates it.
CC       {ECO:0000250|UniProtKB:P06493}.
CC   -!- SUBUNIT: Forms a stable but non-covalent complex with cyclin B in
CC       mature oocytes. {ECO:0000250|UniProtKB:P51958}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P06493}.
CC       Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC       {ECO:0000250|UniProtKB:P06493}.
CC   -!- PTM: Phosphorylation at Tyr-15 by wee1 and wee2 inhibits the protein
CC       kinase activity and acts negative regulator of entry into mitosis (G2
CC       to M transition). {ECO:0000250|UniProtKB:P06493}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC       protein kinase family. CDC2/CDKX subfamily. {ECO:0000305}.
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DR   EMBL; AB050458; BAB17216.1; -; mRNA.
DR   AlphaFoldDB; Q9DGA5; -.
DR   SMR; Q9DGA5; -.
DR   GO; GO:0005813; C:centrosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; ISS:UniProtKB.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0008353; F:RNA polymerase II CTD heptapeptide repeat kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0000086; P:G2/M transition of mitotic cell cycle; ISS:UniProtKB.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd07861; STKc_CDK1_euk; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR24056; CELL DIVISION PROTEIN KINASE; 1.
DR   PANTHER; PTHR24056:SF334; CYCLIN-DEPENDENT KINASE 1; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Cell cycle; Cell division; Cytoplasm; Cytoskeleton; Kinase;
KW   Mitosis; Nucleotide-binding; Nucleus; Phosphoprotein;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..303
FT                   /note="Cyclin-dependent kinase 1"
FT                   /id="PRO_0000085730"
FT   DOMAIN          4..287
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   ACT_SITE        128
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         10..18
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         33
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         14
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P06493"
FT   MOD_RES         15
FT                   /note="Phosphotyrosine; by wee1 and wee2"
FT                   /evidence="ECO:0000250|UniProtKB:P06493"
FT   MOD_RES         161
FT                   /note="Phosphothreonine; by cak"
FT                   /evidence="ECO:0000250|UniProtKB:P06493"
SQ   SEQUENCE   303 AA;  34605 MW;  65ECD9A989248B8F CRC64;
     MEDYVKIEKI GEGTYGVVYK GRHKSTGQVV AMKKIRLESE EEGVPSTAVR EVSLLQELKH
     PNVVRLLDVL MQESRLYLIF EFLSMDLKKY LDSIPSGQYM DPMLVKSYLY QILEGIYFCH
     RRRVLHRDLK PQNLLIDNKG VIKLADFGLS RAFGVPVRVY THEVVTLWYR APEVLLGSPR
     YSTPVDVWST GTIFAELATK KPLFHGDSEI DQLFRIFRTL GTPNNDVWPD VESLPDYKST
     FPKWKGGSLS SMVKNLDKNG LDLLAKMLIY NPPKRISARE AMTHPYFDDL DKSTLPAACI
     NGV
//